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. 2009 Mar 6;5(3):e1000330. doi: 10.1371/journal.ppat.1000330

Figure 3. Oligomerization of wild type and mutant A3G proteins.

Figure 3

(A) Co-immunoprecipitation of wild type and mutant A3G with HA-tagged wild type A3G (A3G-HA). Immunoblots on the left show whole cell expression of A3G, A3G-HA, and the cellular control protein Hsp90. On the right, blots show A3G and A3G-HA in the immunoprecipitate, with or without RNase A treatment. (B) Immunoblot showing A3G after chemical crosslinking with BM(PEO)3 in the lysate of transfected 293T cells. Lane 1, untreated control; lane 2, BM(PEO)3 treated; lane 3, BM(PEO)3 treated after incubation with RNase A; lane 4, BM(PEO)3 treated before incubation with RNase A. Relative molecular mass markers (in kD) are indicated on the right. (C) Immunoblot showing the immunoprecipitation of myc-tagged A3G (A3G-myc) with A3G-HA, with or without BM(PEO)3 and subsequent RNase A treatment. Samples were immunoprecipitated with anti-HA antibody, and immoblots were probed with the anti-myc antibody. An asterisk indicates the position of a band generated by crossreactivity to the heavy chain of the 3F10 antibody used for immunoprecipitation. (D) Immunoblot showing the effect of BM(PEO)3 treatment on wild type and mutant A3G in the lysates of transfected 293T cells. The control sample transfected with the empty vector is indicated by -.